5hvx
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Full length Wild-Type Open-form Sodium Channel NavMs== | |
| + | <StructureSection load='5hvx' size='340' side='right' caption='[[5hvx]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5hvx]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HVX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HVX FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=12P:DODECAETHYLENE+GLYCOL'>12P</scene>, <scene name='pdbligand=2CV:HEGA-10'>2CV</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5hvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hvx OCA], [http://pdbe.org/5hvx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hvx RCSB], [http://www.ebi.ac.uk/pdbsum/5hvx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hvx ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Voltage-gated sodium channels (Navs) play essential roles in excitable tissues, with their activation and opening resulting in the initial phase of the action potential. The cycling of Navs through open, closed and inactivated states, and their closely choreographed relationships with the activities of other ion channels lead to exquisite control of intracellular ion concentrations in both prokaryotes and eukaryotes. Here we present the 2.45 A resolution crystal structure of the complete NavMs prokaryotic sodium channel in a fully open conformation. A canonical activated conformation of the voltage sensor S4 helix, an open selectivity filter leading to an open activation gate at the intracellular membrane surface and the intracellular C-terminal domain are visible in the structure. It includes a heretofore unseen interaction motif between W77 of S3, the S4-S5 interdomain linker, and the C-terminus, which is associated with regulation of opening and closing of the intracellular gate. | ||
| - | + | The complete structure of an activated open sodium channel.,Sula A, Booker J, Ng LC, Naylor CE, DeCaen PG, Wallace BA Nat Commun. 2017 Feb 16;8:14205. doi: 10.1038/ncomms14205. PMID:28205548<ref>PMID:28205548</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5hvx" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Booker, J E]] | ||
| + | [[Category: Naylor, C E]] | ||
| + | [[Category: Sula, A]] | ||
| + | [[Category: Wallace, B A]] | ||
| + | [[Category: Integral membrane full length voltage gated sodium channel transport]] | ||
| + | [[Category: Transport protein]] | ||
Revision as of 09:32, 11 March 2017
Full length Wild-Type Open-form Sodium Channel NavMs
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